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Molecular Microbiology|January 14, 1998
The outer membrane component, YscC, of the Yop secretion machinery of Yersinia enterocolitica forms a ring-shaped multimeric complexM Koster, W Bitter, H de Cock, et al.Cellular and Molecular Life Sciences : CMLS|December 12, 2002
SecB, one small chaperone in the complex milieu of the cellL L Randall, S J S HardyThe EMBO Journal|December 18, 2001
Outer membrane composition of a lipopolysaccharide-deficient Neisseria meningitidis mutantL Steeghs, H de Cock, E Evers, et al.The Journal of Biological Chemistry|March 30, 2001
The early interaction of the outer membrane protein phoe with the periplasmic chaperone Skp occurs at the cytoplasmic membraneN Harms, G Koningstein, W Dontje, et al.Biochimica Et Biophysica Acta|March 23, 2000
Biochemical and biophysical characterization of in vitro folded outer membrane porin PorA of Neisseria meningitidisC Jansen, A Wiese, L Reubsaet, et al.Journal of Protein Chemistry|October 1, 1995
Chaperone SecB: conformational changes demonstrated by circular dichroismG D Fasman, K Park, L L RandallProceedings of the National Academy of Sciences of the United States of America|December 1, 1989
Physiological role during export for the retardation of folding by the leader peptide of maltose-binding proteinG Liu, T B Topping, L L RandallFEMS Immunology and Medical Microbiology|February 23, 2000
Immunogenicity of in vitro folded outer membrane protein PorA of Neisseria meningitidisC Jansen, B Kuipers, J van der Biezen, et al.Proceedings of the National Academy of Sciences of the United States of America|March 1, 1978
Precursors of three exported proteins in Escherichia coliL L Randall, S J Hardy, L G JosefssonEuropean Journal of Biochemistry|June 1, 1980
Novel intermediates in the synthesis of maltose-binding protein in Escherichia coliL L Randall, L G Josefsson, S J HardyPageof 11